941292-88-2Relevant articles and documents
Differential Effects of β3- versus β2-Amino Acid Residues on the Helicity and Recognition Properties of Bim BH3-Derived α/β-Peptides
Eddinger, Geoffrey A.,Gellman, Samuel H.
, p. 13829 - 13832 (2018)
Oligomers containing α- and β-amino acid residues (α/β-peptides) have been shown to mimic the α-helical conformation of conventional peptides when the unnatural residues are derived from β3-amino acids or cyclic β-amino acids, but the impact of incorporating β2 residues has received little attention. The effects of β2 residues on the conformation and recognition behavior of α/β-peptides that mimic an isolated α-helix were investigated. This effort has focused on 26-mers based on the Bim BH3 domain; a set of isomers with identical α/β backbones that differ only in the placement of certain side chains along the backbone (β3 vs. β2 substitution) was compared. Circular dichroism data suggest that β2 residues can be helix-destabilizing relative to β3 residues, although the size of this effect seems to depend on side chain identity. Binding data show that β3→β2 substitution at sites that contact a partner protein, Bcl-xL, can influence affinity in a way that transcends effects on helicity.
Practical synthesis of enantiomerically pure β2-amino acids via proline-catalyzed diastereoselective aminomethylation of aldehydes
Chi, Yonggui,English, Emily P.,Pomerantz, William C.,Horne, W. Seth,Joyce, Leo A.,Alexander, Lane R.,Fleming, William S.,Hopkins, Elizabeth A.,Gellman, Samuel H.
, p. 6050 - 6055 (2008/02/08)
Proline-catalyzed diastereoselective aminomethylation of aldehydes using a chiral iminium ion, generated from a readily prepared precursor, provides α-substituted-β-amino aldehydes with 85:15 to 90: 10 dr. The α-substituted-β-amino aldehydes can be reduce
